Evidence map›Paper›PMID 26755740›Full record

ArticlePhysiological reports2016

Orai1 forms a signal complex with BKCa channel in mesenteric artery smooth muscle cells.

Meihua Chen, Jie Li, Feifei Jiang, Jie Fu, Xianming Xia, Juan Du, Min Hu, Junhao Huang, Bing Shen

Open access · goldAbstract read
In one paragraph

Article in Physiological reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Enhanced Store-Operated CaFrontiers in physiology · 2021
    Article
  6. Review
  7. TRPP2 and STIM1 form a microdomain to regulate store-operated CaCell communication and signaling : CCS · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. STIM Proteins and Orai CaFrontiers in pharmacology · 2018
    Article
  13. Review
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Meihua ChenDepartment of Physiology, Anhui Medical University, Hefei, Anhui, China.
Jie LiDepartment of Physiology, Anhui Medical University, Hefei, Anhui, China.
Feifei JiangDepartment of Pediatrics, The people's hospital of Bozhou, Bozhou, Anhui, China.
Jie FuDepartment of Physiology, Anhui Medical University, Hefei, Anhui, China.
Xianming XiaDepartment of Gastroenterology and Hepatology, The Fourth Affiliated Hospital of Anhui Medical University, Hefei, Anhui, China.
Juan DuDepartment of Physiology, Anhui Medical University, Hefei, Anhui, China.
Min HuDepartment of Sports and Health, Guangdong Provincial Key Laboratory of Sports and Health Promotion, Guangzhou Sport University, Guangzhou, Guangdong, China.
Junhao HuangDepartment of Sports and Health, Guangdong Provincial Key Laboratory of Sports and Health Promotion, Guangzhou Sport University, Guangzhou, Guangdong, China shenbing@ahmu.edu.cn junhaohuang2006@hotmail.com.
Bing ShenDepartment of Physiology, Anhui Medical University, Hefei, Anhui, China Central Laboratory of Molecular and Cellular Biology of School of Basic Medicine, Anhui Medical University, Hefei, Anhui, China shenbing@ahmu.edu.cn junhaohuang2006@hotmail.com.
Anhui Medical University · CNGuangzhou Sport University · CNBozhou People's Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Orai1, a specific nonvoltage-gated Ca(2+) channel, has been found to be one of key molecules involved in store-operated Ca(2+) entry (SOCE). Orai1 may associate with other proteins to form a signaling complex, which is essential for regulating a variety of physiological functions. In this study, we studied the possible interaction between Orai1 and large conductance Ca(2+)-activated potassium channel (BKC a). Using RNA interference technique, we demonstrated that the SOCE and its associated membrane hyperpolarization were markedly suppressed after knockdown of Orai1 with a specific Orai1 siRNA in rat mesenteric artery smooth muscle. Moreover, isometric tension measurements showed that agonist-induced vasocontraction was increased after Orai1 was knocked down or the tissue was incubated with BKC a blocker iberiotoxin. Coimmunoprecipitation data revealed that BKC a and Orai1 could reciprocally pull down each other. In situ proximity ligation assay further demonstrated that Orai1 and BKC a are in close proximity. Taken together, these results indicate that Orai1 physically associates with BKC a to form a signaling complex in the rat mesenteric artery smooth muscle. Ca(2+) influx via Orai1 stimulates BKC a, leading to membrane hyperpolarization. This hyperpolarizing effect of Orai1-BKC a coupling could contribute to reduce agonist-induced membrane depolarization, therefore preventing excessive contraction of the rat mesenteric artery smooth muscle in response to contractile agonists.

Indexed as

AnimalsCalcium ChannelsCells, CulturedLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMembrane PotentialsMesenteric ArteriesMuscle, Smooth, VascularMyocytes, Smooth MuscleORAI1 ProteinOrgan Culture TechniquesPhenylephrineRatsRats, Sprague-DawleyVasoconstrictionCalcium ChannelsKcnma1 protein, ratLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsORAI1 ProteinOrai1 protein, ratPhenylephrineBKC amesenteric arteryOrai1store‐operated Ca2+ entryvascular smooth muscle cells

Identifiers

PMID26755740
PMCPMC4760400
OpenAlexW2280566736

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.